Evidence map›Paper›PMID 11003661›Full record

ArticleMolecular and cellular biology2000

Regulation of yeast H(+)-ATPase by protein kinases belonging to a family dedicated to activation of plasma membrane transporters.

A Goossens, N de La Fuente, J Forment, R Serrano, F Portillo

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

82 citing papers in PubMed, 187 citations in OpenAlex.

  1. Evolution of cross-tolerance to metals in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The Ptk2-Pma1 pathway enhances tolerance to terbinafine inAntimicrobial agents and chemotherapy · 2024
    Article
  9. Fungal Plasma Membrane HJournal of fungi (Basel, Switzerland) · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Journal of fungi (Basel, Switzerland) · 2022
    Article
  19. Article
  20. Article

22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

A GoossensInstituto de Biologia Molecular y Celular de Plantas, Universidad Politecnica de Valencia-C.S.I.C., 46022 Valencia, Spain.
N de La Fuente
J Forment
R Serrano
F Portillo
Instituto de Biología Molecular y Celular de Plantas · ESUniversidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The regulation of electrical membrane potential is a fundamental property of living cells. This biophysical parameter determines nutrient uptake, intracellular potassium and turgor, uptake of toxic cations, and stress responses. In fungi and plants, an important determinant of membrane potential is the electrogenic proton-pumping ATPase, but the systems that modulate its activity remain largely unknown. We have characterized two genes from Saccharomyces cerevisiae, PTK2 and HRK1 (YOR267c), that encode protein kinases implicated in activation of the yeast plasma membrane H(+)-ATPase (Pma1) in response to glucose metabolism. These kinases mediate, directly or indirectly, an increase in affinity of Pma1 for ATP, which probably involves Ser-899 phosphorylation. Ptk2 has the strongest effect on Pma1, and ptk2 mutants exhibit a pleiotropic phenotype of tolerance to toxic cations, including sodium, lithium, manganese, tetramethylammonium, hygromycin B, and norspermidine. A plausible interpretation is that ptk2 mutants have a decreased membrane potential and that diverse cation transporters are voltage dependent. Accordingly, ptk2 mutants exhibited reduced uptake of lithium and methylammonium. Ptk2 and Hrk1 belong to a subgroup of yeast protein kinases dedicated to the regulation of plasma membrane transporters, which include Npr1 (regulator of Gap1 and Tat2 amino acid transporters) and Hal4 and Hal5 (regulators of Trk1 and Trk2 potassium transporters).

Indexed as

Saccharomyces cerevisiae ProteinsAdenosine TriphosphateAmino Acid Transport SystemsCarrier ProteinsCationsCell MembraneCloning, MolecularEnzyme ActivationFocal Adhesion Protein-Tyrosine KinasesFungal ProteinsGlucoseHygromycin BIsoenzymesKineticsLithiumMembrane PotentialsAdenosine TriphosphateAmino Acid Transport SystemsCarrier ProteinsCationsFocal Adhesion Protein-Tyrosine KinasesFungal ProteinsGlucoseHRK1 protein, S cerevisiaeHygromycin BIsoenzymesLithiumPhosphoserinePMA1 protein, S cerevisiaePMA2 protein, S cerevisiaePotassium ChannelsProtein KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProton-Translocating ATPasesSaccharomyces cerevisiae Proteins

Identifiers

PMID11003661
PMCPMC86331
OpenAlexW2127710730

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.